ID A0A540L0N1_MALBA Unreviewed; 1131 AA.
AC A0A540L0N1;
DT 16-OCT-2019, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2019, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Chromatin-remodeling complex ATPase {ECO:0008006|Google:ProtNLM};
GN ORFNames=C1H46_034407 {ECO:0000313|EMBL:TQD80034.1};
OS Malus baccata (Siberian crab apple) (Pyrus baccata).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Rosaceae; Amygdaloideae; Maleae; Malus.
OX NCBI_TaxID=106549 {ECO:0000313|EMBL:TQD80034.1, ECO:0000313|Proteomes:UP000315295};
RN [1] {ECO:0000313|EMBL:TQD80034.1, ECO:0000313|Proteomes:UP000315295}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Shandingzi {ECO:0000313|Proteomes:UP000315295};
RC TISSUE=Leaves {ECO:0000313|EMBL:TQD80034.1};
RA Chen X.;
RT "Sequencing of a Wild Apple (Malus baccata) Genome Unravels the Differences
RT Between Cultivated and Wild Apple Species Regarding Disease Resistance and
RT Cold Tolerance.";
RL G3 (Bethesda) 9:1785-1793(2019).
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. ISWI subfamily.
CC {ECO:0000256|ARBA:ARBA00009687}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:TQD80034.1}.
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DR EMBL; VIEB01000825; TQD80034.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A540L0N1; -.
DR STRING; 106549.A0A540L0N1; -.
DR Proteomes; UP000315295; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0031491; F:nucleosome binding; IEA:InterPro.
DR CDD; cd17997; DEXHc_SMARCA1_SMARCA5; 1.
DR CDD; cd00167; SANT; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 1.10.10.60; Homeodomain-like; 2.
DR Gene3D; 1.20.5.1190; iswi atpase; 1.
DR Gene3D; 1.10.1040.30; ISWI, HAND domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 1.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR044754; Isw1/2_DEXHc.
DR InterPro; IPR015194; ISWI_HAND-dom.
DR InterPro; IPR036306; ISWI_HAND-dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001005; SANT/Myb.
DR InterPro; IPR017884; SANT_dom.
DR InterPro; IPR015195; SLIDE.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR049730; SNF2/RAD54-like_C.
DR InterPro; IPR000330; SNF2_N.
DR PANTHER; PTHR45623; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 3-RELATED-RELATED; 1.
DR PANTHER; PTHR45623:SF49; SWI_SNF RELATED, MATRIX ASSOCIATED, ACTIN DEPENDENT REGULATOR OF CHROMATIN, SUBFAMILY A, MEMBER 1; 1.
DR Pfam; PF09110; HAND; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF09111; SLIDE; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00717; SANT; 2.
DR SUPFAM; SSF101224; HAND domain of the nucleosome remodeling ATPase ISWI; 1.
DR SUPFAM; SSF46689; Homeodomain-like; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS51293; SANT; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000315295}.
FT DOMAIN 212..377
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 505..656
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 839..891
FT /note="SANT"
FT /evidence="ECO:0000259|PROSITE:PS51293"
FT REGION 1..91
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 149..172
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1011..1053
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..24
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 25..46
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 53..81
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1011..1028
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1131 AA; 130903 MW; DABB713AEF7D9E14 CRC64;
MARASKPQVS SDEAPSNGFN SSEEEPINDQ EEEEVDEEEL EAVARTADSD DDENYPGSDD
DMVADENGDD GLEEEEDDEA SLSNAEIGKR EKARLRDMQN LKRQKVQEIL DAQNAAIEAD
MNNKGKGRLK YLLRQTELFA HFAKGDQSAS QKKVKGKGRH ASKLTEEEED EECLKEEEDG
LAGAGTTRLL TQPSCIQGKM RDYQLAGLNW LIRLYENGIN GILADEMGLG KTLQTISLLG
YLHEFRGITG PHMVVAPKST LGNWMNEIRR FCPILRAVKF LGNPDERKHI REDLLVAGNF
DVCVTSFEMA IKEKTCLRRF SWRYIIIDEA HRIKNENSLL SKTMRLYNTN FRLLITGTPL
QNNLHELWSL LNFLLPEIFS SAETFDEWFQ ISGENDQQEV VQQLHKVLRP FLLRRLKSDV
EKGLPPKKET ILKVGMSQMQ KQYYRALLQK DLEVVNAGGE RKRLLNIAMQ LRKCCNHPYL
FQGAEPGPPY TTGDHLITSA GKMVLLDKLL PKLKERDSRV LIFSQMTRLL DILEDYLMLR
GYLYCRIDGN TGGEDRDASI DAFNKPGSEK FVFLLSTRAG GLGINLATAD VVILYDSDWN
PQVDLQAQDR AHRIGQKKEV QVFRFCTEYT IEEKVIERAY KKLALDALVI QQGRLAEQKT
VNKDELLQMV RFGAEMVFSS KDSTITDEDI DRIIAKGEET TAELDAKMKK FTEDAIKFKM
DDTAELYDFD DEKDDKLDFK KIVSDNWIEP PKRERKRNYS ESEYFKQTMR QGAPAKPREP
RIPRMPQLHD FQFFHTQRLN ELYEKEVRFL MQTHQKNQLK DTIEVEEPEE VGDPLTAEEG
FSTWSRRDFN TFIRACEKYG RNDIKSIAAE MEGKTEEEVE RYAKVFKERY KELNDYDRII
KNIERGEARI SRKDEIMKAI GKKLDRYKNP WLELKIQYGQ NKGKLYNEEC DRFMLCMVHK
LGYGNWDELK AEFRTSPLFR FDWFVKSRTT QELARRCDTI IRLVEKENQE YDERERQARK
EKKLAKSMAP SKRAMGRQPT ESPNSGKKRK QPTMDDYVNS ITVRFNITCD RSSDRDLSSV
RFLSVAVAVY ISSESLMILV DVWLVKLTRA VSYIVYAELK GFSRLWFSSK G
//
